NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|496082082|ref|WP_008806589|]
View 

MULTISPECIES: glutathione S-transferase family protein [Klebsiella]

Protein Classification

glutathione S-transferase family protein( domain architecture ID 11418207)

glutathione S-transferase family protein similar to Saccharomyces cerevisiae glutathione S-transferase omega-like proteins and Escherichia coli glutathionyl-hydroquinone reductase

CATH:  1.20.1050.10|3.40.30.10
EC:  1.8.5.-
Gene Ontology:  GO:0016491|GO:0004364
PubMed:  20388120|15822171|16839810|9074797
SCOP:  4000976|4000472

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ECM4 COG0435
Glutathionyl-hydroquinone reductase [Energy production and conversion];
1-328 0e+00

Glutathionyl-hydroquinone reductase [Energy production and conversion];


:

Pssm-ID: 440204 [Multi-domain]  Cd Length: 321  Bit Score: 658.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082   1 MGQLVDGVWQDTWYDTKSTGGRFKRSVSAFRNWLTADGAPGpageggFAAEKDRYHLYVSLACPWAHRTLILRKLKGLEP 80
Cdd:COG0435    1 MGLLVDGKWHDDWYDTKDTGGRFVRQESQFRNWITADGSGG------FPAEAGRYHLYVSLACPWAHRTLIFRALKGLED 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082  81 FISVSVVNPLMLENGWTFaDDFPGATGDQLYHHQFLYQLYLQADPHYTGRVTVPVLWDKKQQTIVSNESAEIIRMFNTAF 160
Cdd:COG0435   75 AISVSVVHPLMLEDGWTF-SPDPGATPDPLNGARYLHELYTKADPDYTGRVTVPVLWDKQTGTIVNNESAEIIRMLNSAF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082 161 DGLGARAGDYYPPALREKIDELNGWIYDNVNNGVYKAGFATSQQAYDEAVEAVFTSLERLEQILGQHRYLTGNQLTEADI 240
Cdd:COG0435  154 DGLAGNDLDLYPEALREEIDALNDRIYDTVNNGVYRAGFATTQEAYEEAVDELFDALDWLEERLSDQRYLCGDRLTEADW 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082 241 RLWTTLVRFDPVYVTHFKCDKRRISDYLNLYGFLRDIYQMPGIAETVSIPHIRHHYYRSHKTINPTGIISIGPQQDLNEP 320
Cdd:COG0435  234 RLFTTLVRFDAVYHGHFKCNRRRIADYPNLWGYLRDLYQLPGVAETVDFDHIKRHYYGSHPTINPTGIVPLGPDLDLDAP 313


                 ....*...
gi 496082082 321 HGRDQRFR 328
Cdd:COG0435  314 HDRDRLGG 321
 
Name Accession Description Interval E-value
ECM4 COG0435
Glutathionyl-hydroquinone reductase [Energy production and conversion];
1-328 0e+00

Glutathionyl-hydroquinone reductase [Energy production and conversion];


Pssm-ID: 440204 [Multi-domain]  Cd Length: 321  Bit Score: 658.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082   1 MGQLVDGVWQDTWYDTKSTGGRFKRSVSAFRNWLTADGAPGpageggFAAEKDRYHLYVSLACPWAHRTLILRKLKGLEP 80
Cdd:COG0435    1 MGLLVDGKWHDDWYDTKDTGGRFVRQESQFRNWITADGSGG------FPAEAGRYHLYVSLACPWAHRTLIFRALKGLED 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082  81 FISVSVVNPLMLENGWTFaDDFPGATGDQLYHHQFLYQLYLQADPHYTGRVTVPVLWDKKQQTIVSNESAEIIRMFNTAF 160
Cdd:COG0435   75 AISVSVVHPLMLEDGWTF-SPDPGATPDPLNGARYLHELYTKADPDYTGRVTVPVLWDKQTGTIVNNESAEIIRMLNSAF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082 161 DGLGARAGDYYPPALREKIDELNGWIYDNVNNGVYKAGFATSQQAYDEAVEAVFTSLERLEQILGQHRYLTGNQLTEADI 240
Cdd:COG0435  154 DGLAGNDLDLYPEALREEIDALNDRIYDTVNNGVYRAGFATTQEAYEEAVDELFDALDWLEERLSDQRYLCGDRLTEADW 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082 241 RLWTTLVRFDPVYVTHFKCDKRRISDYLNLYGFLRDIYQMPGIAETVSIPHIRHHYYRSHKTINPTGIISIGPQQDLNEP 320
Cdd:COG0435  234 RLFTTLVRFDAVYHGHFKCNRRRIADYPNLWGYLRDLYQLPGVAETVDFDHIKRHYYGSHPTINPTGIVPLGPDLDLDAP 313


                 ....*...
gi 496082082 321 HGRDQRFR 328
Cdd:COG0435  314 HDRDRLGG 321
GST_C_Omega_like cd03190
C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione ...
 172-313 1.32e-81

C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast.


Pssm-ID: 198299 [Multi-domain]  Cd Length: 142  Bit Score: 244.02  E-value: 1.32e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082 172 PPALREKIDELNGWIYDNVNNGVYKAGFATSQQAYDEAVEAVFTSLERLEQILGQHRYLTGNQLTEADIRLWTTLVRFDP 251
Cdd:cd03190    1 PEELRKEIDELNEWIYDNINNGVYKAGFATTQEAYDKAVKELFEALDKLEKRLSKQPYLLGDRLTEADIRLFTTLIRFDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082082 252 VYVTHFKCDKRRISDYLNLYGFLRDIYQMPGIAETVSIPHIRHHYYRSHKTINPTGIISIGP 313
Cdd:cd03190   81 VYHQHFKCNLKTIRDYPNLWRYLRRLYQNPGVFETTNFDHIKQHYYGSHFPINPNGIVPAGP 142
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 205-268 4.98e-10

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 55.02  E-value: 4.98e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082082  205 AYDEAVEAVFTSLERLEQILGQHRYLTGNQLTEADIRLWTTLVRFDPVYVTHFKCDKR-RISDYL 268
Cdd:pfam13410   1 ALERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDLREGYpRLRAWL 65
 
Name Accession Description Interval E-value
ECM4 COG0435
Glutathionyl-hydroquinone reductase [Energy production and conversion];
1-328 0e+00

Glutathionyl-hydroquinone reductase [Energy production and conversion];


Pssm-ID: 440204 [Multi-domain]  Cd Length: 321  Bit Score: 658.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082   1 MGQLVDGVWQDTWYDTKSTGGRFKRSVSAFRNWLTADGAPGpageggFAAEKDRYHLYVSLACPWAHRTLILRKLKGLEP 80
Cdd:COG0435    1 MGLLVDGKWHDDWYDTKDTGGRFVRQESQFRNWITADGSGG------FPAEAGRYHLYVSLACPWAHRTLIFRALKGLED 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082  81 FISVSVVNPLMLENGWTFaDDFPGATGDQLYHHQFLYQLYLQADPHYTGRVTVPVLWDKKQQTIVSNESAEIIRMFNTAF 160
Cdd:COG0435   75 AISVSVVHPLMLEDGWTF-SPDPGATPDPLNGARYLHELYTKADPDYTGRVTVPVLWDKQTGTIVNNESAEIIRMLNSAF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082 161 DGLGARAGDYYPPALREKIDELNGWIYDNVNNGVYKAGFATSQQAYDEAVEAVFTSLERLEQILGQHRYLTGNQLTEADI 240
Cdd:COG0435  154 DGLAGNDLDLYPEALREEIDALNDRIYDTVNNGVYRAGFATTQEAYEEAVDELFDALDWLEERLSDQRYLCGDRLTEADW 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082 241 RLWTTLVRFDPVYVTHFKCDKRRISDYLNLYGFLRDIYQMPGIAETVSIPHIRHHYYRSHKTINPTGIISIGPQQDLNEP 320
Cdd:COG0435  234 RLFTTLVRFDAVYHGHFKCNRRRIADYPNLWGYLRDLYQLPGVAETVDFDHIKRHYYGSHPTINPTGIVPLGPDLDLDAP 313


                 ....*...
gi 496082082 321 HGRDQRFR 328
Cdd:COG0435  314 HDRDRLGG 321
GST_C_Omega_like cd03190
C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione ...
 172-313 1.32e-81

C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast.


Pssm-ID: 198299 [Multi-domain]  Cd Length: 142  Bit Score: 244.02  E-value: 1.32e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082 172 PPALREKIDELNGWIYDNVNNGVYKAGFATSQQAYDEAVEAVFTSLERLEQILGQHRYLTGNQLTEADIRLWTTLVRFDP 251
Cdd:cd03190    1 PEELRKEIDELNEWIYDNINNGVYKAGFATTQEAYDKAVKELFEALDKLEKRLSKQPYLLGDRLTEADIRLFTTLIRFDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082082 252 VYVTHFKCDKRRISDYLNLYGFLRDIYQMPGIAETVSIPHIRHHYYRSHKTINPTGIISIGP 313
Cdd:cd03190   81 VYHQHFKCNLKTIRDYPNLWRYLRRLYQNPGVFETTNFDHIKQHYYGSHFPINPNGIVPAGP 142
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 205-268 4.98e-10

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 55.02  E-value: 4.98e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082082  205 AYDEAVEAVFTSLERLEQILGQHRYLTGNQLTEADIRLWTTLVRFDPVYVTHFKCDKR-RISDYL 268
Cdd:pfam13410   1 ALERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDLREGYpRLRAWL 65
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 62-159 1.88e-09

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 53.40  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082   62 ACPWAHRTLILRKLKGLePFIsVSVVNPLMLENGWTFADdfpgatgdqlyhhqflyqlylqadphYTGRVTVPVLWDKKQ 141
Cdd:pfam13409   1 FSPFSHRVRLALEEKGL-PYE-IELVDLDPKDKPPELLA--------------------------LNPLGTVPVLVLPDG 52

                          90
                  ....*....|....*...
gi 496082082  142 QTIvsNESAEIIRMFNTA 159
Cdd:pfam13409  53 TVL--TDSLVILEYLEEL 68
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 176-252 2.93e-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: 50.96  E-value: 2.93e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496082082 176 REKIDELNGWIYDNVNNGVYKAGF--ATSQQAYDEAVEAVFTSLERLEQILGQHRYLTGNQLTEADIRLWTTLVRFDPV 252
Cdd:cd00299    2 RALEDWADATLAPPLVRLLYLEKVplPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAL 80
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
57-287 2.22e-07

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 50.66  E-value: 2.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082  57 LYVSLACPWAHRTLILRKLKGLePFISVSVVnplmLENGWTFADDFpgatgdqlyhhqflyqlyLQADPhyTGRVtvPVL 136
Cdd:COG0625    4 LYGSPPSPNSRRVRIALEEKGL-PYELVPVD----LAKGEQKSPEF------------------LALNP--LGKV--PVL 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082 137 WDKkqQTIVSnESAEIIRMFNTAFDGlgaraGDYYPPALREK------IDELNGWIYDNVNNGVYKAGFATSQQAYDEAV 210
Cdd:COG0625   57 VDD--GLVLT-ESLAILEYLAERYPE-----PPLLPADPAARarvrqwLAWADGDLHPALRNLLERLAPEKDPAAIARAR 128

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082082 211 EAVFTSLERLEQILGQHRYLTGNQLTEADIRLWTTLVRFDpvyvtHFKCDkrrISDYLNLYGFLRDIYQMPGIAETV 287
Cdd:COG0625  129 AELARLLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLD-----RLGLD---LADYPNLAAWLARLAARPAFQRAL 197
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 195-240 1.12e-04

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: 40.35  E-value: 1.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 496082082  195 YKAGFATSQQAYDEAVEAVFTSLERLEQILGQHRYLTGNQLTEADI 240
Cdd:pfam00043  13 YVPPEEKKEPEVDEALEKVARVLSALEEVLKGQTYLVGDKLTLADI 58
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 217-285 2.87e-04

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 39.46  E-value: 2.87e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082082  217 LERLEQILGQH--RYLTGNQLTEADIRLwttlvrFDPVYVTHFKCDKRRISDYLNLYGFLRDIYQMPGIAE 285
Cdd:pfam14497  35 LGYFEKVLNKNggGYLVGDKLTYADLAL------FQVLDGLLYPKAPDALDKYPKLKALHERVAARPNIKA 99
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 203-249 3.71e-03

Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds to membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.


Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 36.77  E-value: 3.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 496082082 203 QQAYDEAVEAVFTSLERLEQILGQHRYLTGNQLTEADIRLWTTLVRF 249
Cdd:cd03181   35 KKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLRG 81
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
 207-250 4.32e-03

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


Pssm-ID: 198287 [Multi-domain]  Cd Length: 117  Bit Score: 36.36  E-value: 4.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 496082082 207 DEAVEAVFTSLERLEQILGQHRYLTGNQLTEADIRLWTTLVRFD 250
Cdd:cd03177   37 EEKLDKLEEALEFLETFLEGSDYVAGDQLTIADLSLVATVSTLE 80
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 190-285 5.59e-03

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: 36.07  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082082 190 VNNGVYKAGFA-------TSQQAYDE----AVEAVFTSLERLEQILGQHRYLTGNQLTEADIRL-----WTTLVRFDPvy 253
Cdd:cd03188   13 IASELHKAFGPlfyparwADDALAEEvkaaARERLERRLAYLDAQLAGGPYLLGDQFSVADAYLfvvlrWARAVGLDL-- 90

                         90       100       110
                 ....*....|....*....|....*....|..
gi 496082082 254 vthfkcdkrriSDYLNLYGFLRDIYQMPGIAE 285
Cdd:cd03188   91 -----------SDWPHLAAYLARVAARPAVQA 111
GST_C_GluProRS_N cd10309
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ...
 197-246 7.88e-03

Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, bifunctional GluRS-Prolyl-tRNA synthetase (GluProRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluProRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluProRS may be involved in protein-protein interactions, mediating the formation of the multi-aaRS complex in higher eukaryotes. The multi-aaRS complex acts as a molecular hub for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198342 [Multi-domain]  Cd Length: 81  Bit Score: 34.99  E-value: 7.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 496082082 197 AGFATSQQAYDEAveavftsLERLEQILGQHRYLTGNQLTEADIRLWTTL 246
Cdd:cd10309   13 AGRLSCDQDFSSA-------LSYLDKALSLRTYLVGNSLTLADFAVWAAL 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH