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Conserved domains on  [gi|2568417735|ref|WP_306574971|]
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hypothetical protein [Oligella urethralis]

Protein Classification

glutathione S-transferase family protein( domain architecture ID 88)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_family super family cl02776
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 81-203 2.19e-25

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.


The actual alignment was detected with superfamily member cd03189:

Pssm-ID: 470672 [Multi-domain]  Cd Length: 123  Bit Score: 97.38  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568417735  81 PPMAHPDYIQYLQWVHYLEATLLPLVEQQSIIHKLGQSRVPFFaRSIMKKTVLNYLNTHIMPELQRQLNYIDQSLAASGW 160
Cdd:cd03189     1 PPPDTAEYADYLYWLHFAEGSLMPPLLLKLVFGKIGEAPPPFF-RPISRKIADKPLQAFINPELKRHLDFLEDHLAKHPY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2568417735 161 TCGSRFCAADIDLAYILLGLEAEAKLLPEHKNIEMFLSAVKER 203
Cdd:cd03189    80 FAGDELTAADIMMSFPLEAALARGPLLEQYPNIAAYLERIEAR 122
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 4-75 1.41e-07

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03046:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 76  Bit Score: 47.88  E-value: 1.41e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2568417735   4 ITIFHLPSTDSFRSIWLACELGLTFQLN--HRQEADEASDS--ETHPLSKAPILLDGNISIATHGAAREYLLSSYD 75
Cdd:cd03046     1 ITLYHLPRSRSFRILWLLEELGLPYELVlyDRGPGEQAPPEylAINPLGKVPVLVDGDLVLTESAAIILYLAEKYG 76
 
Name Accession Description Interval E-value
GST_C_GTT1_like cd03189
C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione ...
 81-203 2.19e-25

C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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: 198298 [Multi-domain]  Cd Length: 123  Bit Score: 97.38  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568417735  81 PPMAHPDYIQYLQWVHYLEATLLPLVEQQSIIHKLGQSRVPFFaRSIMKKTVLNYLNTHIMPELQRQLNYIDQSLAASGW 160
Cdd:cd03189     1 PPPDTAEYADYLYWLHFAEGSLMPPLLLKLVFGKIGEAPPPFF-RPISRKIADKPLQAFINPELKRHLDFLEDHLAKHPY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2568417735 161 TCGSRFCAADIDLAYILLGLEAEAKLLPEHKNIEMFLSAVKER 203
Cdd:cd03189    80 FAGDELTAADIMMSFPLEAALARGPLLEQYPNIAAYLERIEAR 122
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-209 1.29e-16

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 76.09  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568417735   4 ITIFHL-PSTDSFRSIWLACELGLTFQLN--HRQEADEASDS--ETHPLSKAPILLDGNISIATHGAAREYLLSSYDRCG 78
Cdd:COG0625     2 MKLYGSpPSPNSRRVRIALEEKGLPYELVpvDLAKGEQKSPEflALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568417735  79 MRPPmAHPDYIQYLQWVHYLEATLLPLVEQqsIIHKLGQSRVPFFARSIMKktvlnylnthimpELQRQLNYIDQSLAAS 158
Cdd:COG0625    82 LLPA-DPAARARVRQWLAWADGDLHPALRN--LLERLAPEKDPAAIARARA-------------ELARLLAVLEARLAGG 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2568417735 159 GWTCGSRFCAADIDLAYILLGLEAEAKLLPEHKNIEMFLSAVKERATYQLA 209
Cdd:COG0625   146 PYLAGDRFSIADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRA 196
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 4-75 1.41e-07

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: 47.88  E-value: 1.41e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2568417735   4 ITIFHLPSTDSFRSIWLACELGLTFQLN--HRQEADEASDS--ETHPLSKAPILLDGNISIATHGAAREYLLSSYD 75
Cdd:cd03046     1 ITLYHLPRSRSFRILWLLEELGLPYELVlyDRGPGEQAPPEylAINPLGKVPVLVDGDLVLTESAAIILYLAEKYG 76
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 46-176 1.06e-04

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 42.36  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568417735  46 PLSKAPILLDGNISIATHGAA-REYLLSSY-DRCGMRPPMAHPDYiQYLQWVHYLeATLLplveqqsiiHKlGQSrvPFF 123
Cdd:PRK10542   48 PKGQVPALLLDDGTLLTEGVAiMQYLADSVpDRQLLAPVGSLSRY-HTIEWLNYI-ATEL---------HK-GFT--PLF 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2568417735 124 aRSimkKTVLNYLNThIMPELQRQLNYIDQSLAASGWTCGSRFCAADidlAYI 176
Cdd:PRK10542  114 -RP---DTPEEYKPT-VRAQLEKKFQYVDEALADEQWICGQRFTIAD---AYL 158
 
Name Accession Description Interval E-value
GST_C_GTT1_like cd03189
C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione ...
 81-203 2.19e-25

C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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: 198298 [Multi-domain]  Cd Length: 123  Bit Score: 97.38  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568417735  81 PPMAHPDYIQYLQWVHYLEATLLPLVEQQSIIHKLGQSRVPFFaRSIMKKTVLNYLNTHIMPELQRQLNYIDQSLAASGW 160
Cdd:cd03189     1 PPPDTAEYADYLYWLHFAEGSLMPPLLLKLVFGKIGEAPPPFF-RPISRKIADKPLQAFINPELKRHLDFLEDHLAKHPY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2568417735 161 TCGSRFCAADIDLAYILLGLEAEAKLLPEHKNIEMFLSAVKER 203
Cdd:cd03189    80 FAGDELTAADIMMSFPLEAALARGPLLEQYPNIAAYLERIEAR 122
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-209 1.29e-16

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 76.09  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568417735   4 ITIFHL-PSTDSFRSIWLACELGLTFQLN--HRQEADEASDS--ETHPLSKAPILLDGNISIATHGAAREYLLSSYDRCG 78
Cdd:COG0625     2 MKLYGSpPSPNSRRVRIALEEKGLPYELVpvDLAKGEQKSPEflALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568417735  79 MRPPmAHPDYIQYLQWVHYLEATLLPLVEQqsIIHKLGQSRVPFFARSIMKktvlnylnthimpELQRQLNYIDQSLAAS 158
Cdd:COG0625    82 LLPA-DPAARARVRQWLAWADGDLHPALRN--LLERLAPEKDPAAIARARA-------------ELARLLAVLEARLAGG 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2568417735 159 GWTCGSRFCAADIDLAYILLGLEAEAKLLPEHKNIEMFLSAVKERATYQLA 209
Cdd:COG0625   146 PYLAGDRFSIADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRA 196
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 4-75 1.41e-07

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: 47.88  E-value: 1.41e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2568417735   4 ITIFHLPSTDSFRSIWLACELGLTFQLN--HRQEADEASDS--ETHPLSKAPILLDGNISIATHGAAREYLLSSYD 75
Cdd:cd03046     1 ITLYHLPRSRSFRILWLLEELGLPYELVlyDRGPGEQAPPEylAINPLGKVPVLVDGDLVLTESAAIILYLAEKYG 76
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 91-203 3.05e-05

C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.


Pssm-ID: 198316 [Multi-domain]  Cd Length: 101  Bit Score: 41.90  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568417735  91 YLQWVHY----LEATLLPLVEQQSIIHKLGQSRVPFFARSImkKTVLNYLnthimpelqrqlnyiDQSLAASGWTCGSRF 166
Cdd:cd03207     1 YLRWLFFaagtVEPPLLNKALGRFFEPPWGEPAIAAAYGDL--DERLAAL---------------EAALAGRPYLVGERF 63

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2568417735 167 CAADIDLAYiLLGLEAEAKLLPEHKNIEMFLSAVKER 203
Cdd:cd03207    64 SAADLLLAS-VLRWARAFGLLPEYPALRAYVARCTAR 99
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 46-176 1.06e-04

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 42.36  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568417735  46 PLSKAPILLDGNISIATHGAA-REYLLSSY-DRCGMRPPMAHPDYiQYLQWVHYLeATLLplveqqsiiHKlGQSrvPFF 123
Cdd:PRK10542   48 PKGQVPALLLDDGTLLTEGVAiMQYLADSVpDRQLLAPVGSLSRY-HTIEWLNYI-ATEL---------HK-GFT--PLF 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2568417735 124 aRSimkKTVLNYLNThIMPELQRQLNYIDQSLAASGWTCGSRFCAADidlAYI 176
Cdd:PRK10542  114 -RP---DTPEEYKPT-VRAQLEKKFQYVDEALADEQWICGQRFTIAD---AYL 158
 
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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