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Conserved domains on  [gi|1113432218|gb|OJW94268|]
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MAG: glutathione S-transferase [Alicycliphilus sp. 69-12]

Protein Classification

glutathione S-transferase family protein( domain architecture ID 11427749)

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

CATH:  1.20.1050.10|3.40.30.10
EC:  2.5.1.-
Gene Ontology:  GO:0006749|GO:0005515
PubMed:  11035031
SCOP:  4000976|4000472

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-215 5.69e-19

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


:

Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 83.02  E-value: 5.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113432218   4 LILHHYPASPFAHKARCVLGFKRLAWRSVIV---PSVMPKPDVVALTGgYRRTPFLQIGADIYCDTALICDVLEHLRPEP 80
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVdlaKGEQKSPEFLALNP-LGKVPVLVDDGLVLTESLAILEYLAERYPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113432218  81 TLYPPHLkgvsrvfAQWADTTLFTAAMAYNLQPRAAEALFAGFPEGAAQAFsadrramgmahphpQDAAAAYRSYLRRIA 160
Cdd:COG0625    81 PLLPADP-------AARARVRQWLAWADGDLHPALRNLLERLAPEKDPAAI--------------ARARAELARLLAVLE 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113432218 161 NMVEEHDFLFGSEPCVADFATYHPLWFTRQcvpvMADILSATPAVLEWMDRLAAL 215
Cdd:COG0625   140 ARLAGGPYLAGDRFSIADIALAPVLRRLDR----LGLDLADYPNLAAWLARLAAR 190
 
Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-215 5.69e-19

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 83.02  E-value: 5.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113432218   4 LILHHYPASPFAHKARCVLGFKRLAWRSVIV---PSVMPKPDVVALTGgYRRTPFLQIGADIYCDTALICDVLEHLRPEP 80
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVdlaKGEQKSPEFLALNP-LGKVPVLVDDGLVLTESLAILEYLAERYPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113432218  81 TLYPPHLkgvsrvfAQWADTTLFTAAMAYNLQPRAAEALFAGFPEGAAQAFsadrramgmahphpQDAAAAYRSYLRRIA 160
Cdd:COG0625    81 PLLPADP-------AARARVRQWLAWADGDLHPALRNLLERLAPEKDPAAI--------------ARARAELARLLAVLE 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113432218 161 NMVEEHDFLFGSEPCVADFATYHPLWFTRQcvpvMADILSATPAVLEWMDRLAAL 215
Cdd:COG0625   140 ARLAGGPYLAGDRFSIADIALAPVLRRLDR----LGLDLADYPNLAAWLARLAAR 190
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
6-80 1.81e-14

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 67.25  E-value: 1.81e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113432218   6 LHHYPASPFAHKARCVLGFKRLAWRSVIVPSVMPKPDVVALTGgYRRTPFLQIGADIYCDTALICDVLEHLRPEP 80
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNP-LGKVPVLEDDGGILCESLAIIDYLEELYPGP 74
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 4-74 5.53e-05

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: 40.63  E-value: 5.53e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113432218   4 LILHHYPASPFAHKARCVLGFKRLAWRSVIVPSVMPKPDVVALTGGYRRTPFLQIGADIYCDTALICDVLE 74
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
 
Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-215 5.69e-19

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 83.02  E-value: 5.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113432218   4 LILHHYPASPFAHKARCVLGFKRLAWRSVIV---PSVMPKPDVVALTGgYRRTPFLQIGADIYCDTALICDVLEHLRPEP 80
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVdlaKGEQKSPEFLALNP-LGKVPVLVDDGLVLTESLAILEYLAERYPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113432218  81 TLYPPHLkgvsrvfAQWADTTLFTAAMAYNLQPRAAEALFAGFPEGAAQAFsadrramgmahphpQDAAAAYRSYLRRIA 160
Cdd:COG0625    81 PLLPADP-------AARARVRQWLAWADGDLHPALRNLLERLAPEKDPAAI--------------ARARAELARLLAVLE 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113432218 161 NMVEEHDFLFGSEPCVADFATYHPLWFTRQcvpvMADILSATPAVLEWMDRLAAL 215
Cdd:COG0625   140 ARLAGGPYLAGDRFSIADIALAPVLRRLDR----LGLDLADYPNLAAWLARLAAR 190
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
6-80 1.81e-14

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 67.25  E-value: 1.81e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113432218   6 LHHYPASPFAHKARCVLGFKRLAWRSVIVPSVMPKPDVVALTGgYRRTPFLQIGADIYCDTALICDVLEHLRPEP 80
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNP-LGKVPVLEDDGGILCESLAIIDYLEELYPGP 74
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 11-76 1.24e-07

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 48.01  E-value: 1.24e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1113432218  11 ASPFAHKARCVLGFKRLAWRSVIVP--SVMPKPDVVALTgGYRRTPFLQ-IGADIYCDTALICDVLEHL 76
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDldPKDKPPELLALN-PLGTVPVLVlPDGTVLTDSLVILEYLEEL 68
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 4-74 5.53e-05

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: 40.63  E-value: 5.53e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113432218   4 LILHHYPASPFAHKARCVLGFKRLAWRSVIVPSVMPKPDVVALTGGYRRTPFLQIGADIYCDTALICDVLE 74
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 146-211 8.67e-03

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 34.22  E-value: 8.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113432218 146 QDAAAAYRSYLRRIANMVEEHDFLFGSEPCVADFATYHPLWFTRQcVPVMADILSATPAVLEWMDR 211
Cdd:pfam13410   3 ERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDA-AYPGLDLREGYPRLRAWLER 67
 
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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