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Conserved domains on  [gi|219842335|ref|NP_001137153|]
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glutathione S-transferase kappa 1 isoform d [Homo sapiens]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 6-168 5.30e-84

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 cd03021:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 209  Bit Score: 246.50  E-value: 5.30e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335   6 RTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSG--------------------------------- 52
Cdd:cd03021    1 PKIELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGnkppimlpnkakymakdrkrsaeffgvpirqpk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335  53 --------SLSAMRFLTAVNLEHPE----MLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPK 120
Cdd:cd03021   81 dfffmkkgTLTAQRFLTAISEQHPEstltALEALFREFWVRPWSLTEPITESQSISVAADKLGGSAEQAEKLLKAASTPE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 219842335 121 VKNQLKETTEAACRYGAFGLPITVAHVD-GQTHMLFGSDRMELLAHLLG 168
Cdd:cd03021  161 VKNRLKENTDEALKYGAFGLPWIVVTNDkGKTEMFFGSDRFEQVADFLG 209
 
Name Accession Description Interval E-value
DsbA_GSTK cd03021
DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the ...
 6-168 5.30e-84

DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the GST family of enzymes which catalyzes the transfer of the thiol of GSH to electrophilic substrates. It is specifically located in the mitochondria and peroxisomes, unlike other members of the canonical GST family, which are mainly cytosolic. The biological substrates of GSTK are not yet known. It is presumed to have a protective role during respiration when large amounts of reactive oxygen species are generated. GSTK has the same general fold as DsbA, consisting of a thioredoxin domain interrupted by an alpha-helical domain and its biological unit is a homodimer. GSTK is closely related to the bacterial enzyme, 2-hydroxychromene-2-carboxylate (HCCA) isomerase. It shows little sequence similarity to the other members of the GST family.


Pssm-ID: 239319 [Multi-domain]  Cd Length: 209  Bit Score: 246.50  E-value: 5.30e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335   6 RTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSG--------------------------------- 52
Cdd:cd03021    1 PKIELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGnkppimlpnkakymakdrkrsaeffgvpirqpk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335  53 --------SLSAMRFLTAVNLEHPE----MLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPK 120
Cdd:cd03021   81 dfffmkkgTLTAQRFLTAISEQHPEstltALEALFREFWVRPWSLTEPITESQSISVAADKLGGSAEQAEKLLKAASTPE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 219842335 121 VKNQLKETTEAACRYGAFGLPITVAHVD-GQTHMLFGSDRMELLAHLLG 168
Cdd:cd03021  161 VKNRLKENTDEALKYGAFGLPWIVVTNDkGKTEMFFGSDRFEQVADFLG 209
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 7-168 6.11e-44

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 144.11  E-value: 6.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335    7 TVELFYDVLSPYSWLGFEILCRYQNIW-NINLQLRPSLITGIMKDSG--------------------------------- 52
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYgDVKVVYRPFPLAGAKKIGNvgpsnlpvklkymmadlerwaalygiplrfpan 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335   53 ----SLSAMRFLTAVNLEHpeMLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQaqgLLEKIATPKVKNQLKET 128
Cdd:pfam01323  81 flgnSTRANRLALAAGAEG--LAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEE---FDEFLDSPAVKEAVREN 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 219842335  129 TEAACRYGAFGLPITVahVDGQthMLFGSDRMELLAHLLG 168
Cdd:pfam01323 156 TAAAISLGVFGVPTFV--VGGK--MVFGADRLDTLADALA 191
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 7-171 9.07e-04

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 38.33  E-value: 9.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335   7 TVELFYDVLSPYSWLGFEILCRYQNIWNINL-------QLRPSL--------------------------ITGIMKDSG- 52
Cdd:COG2761    3 KIDIFSDVVCPWCYIGKRRLEKALAEFGDDVeirwrpfELNPDMppegedrreyllakgspeqaeqmrahVEEAAAEEGl 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335  53 -----------SLSAMRFLTAVNLE--HPEMLEKasreLWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEkiaTP 119
Cdd:COG2761   83 pfdfdrikppnTFDAHRLLKAAELQgkQDALLEA----LFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLE---SD 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 219842335 120 KVKNQLKETTEAACRYGAFGLPITVahVDGQtHMLFGSDRMELLAHLLGEKW 171
Cdd:COG2761  156 EAAAAVRADEAEARELGVTGVPTFV--FDGK-YAVSGAQPYEVFEQALRQAL 204
 
Name Accession Description Interval E-value
DsbA_GSTK cd03021
DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the ...
 6-168 5.30e-84

DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the GST family of enzymes which catalyzes the transfer of the thiol of GSH to electrophilic substrates. It is specifically located in the mitochondria and peroxisomes, unlike other members of the canonical GST family, which are mainly cytosolic. The biological substrates of GSTK are not yet known. It is presumed to have a protective role during respiration when large amounts of reactive oxygen species are generated. GSTK has the same general fold as DsbA, consisting of a thioredoxin domain interrupted by an alpha-helical domain and its biological unit is a homodimer. GSTK is closely related to the bacterial enzyme, 2-hydroxychromene-2-carboxylate (HCCA) isomerase. It shows little sequence similarity to the other members of the GST family.


Pssm-ID: 239319 [Multi-domain]  Cd Length: 209  Bit Score: 246.50  E-value: 5.30e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335   6 RTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSG--------------------------------- 52
Cdd:cd03021    1 PKIELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGnkppimlpnkakymakdrkrsaeffgvpirqpk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335  53 --------SLSAMRFLTAVNLEHPE----MLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPK 120
Cdd:cd03021   81 dfffmkkgTLTAQRFLTAISEQHPEstltALEALFREFWVRPWSLTEPITESQSISVAADKLGGSAEQAEKLLKAASTPE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 219842335 121 VKNQLKETTEAACRYGAFGLPITVAHVD-GQTHMLFGSDRMELLAHLLG 168
Cdd:cd03021  161 VKNRLKENTDEALKYGAFGLPWIVVTNDkGKTEMFFGSDRFEQVADFLG 209
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 7-168 6.11e-44

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 144.11  E-value: 6.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335    7 TVELFYDVLSPYSWLGFEILCRYQNIW-NINLQLRPSLITGIMKDSG--------------------------------- 52
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYgDVKVVYRPFPLAGAKKIGNvgpsnlpvklkymmadlerwaalygiplrfpan 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335   53 ----SLSAMRFLTAVNLEHpeMLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQaqgLLEKIATPKVKNQLKET 128
Cdd:pfam01323  81 flgnSTRANRLALAAGAEG--LAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEE---FDEFLDSPAVKEAVREN 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 219842335  129 TEAACRYGAFGLPITVahVDGQthMLFGSDRMELLAHLLG 168
Cdd:pfam01323 156 TAAAISLGVFGVPTFV--VGGK--MVFGADRLDTLADALA 191
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 8-167 6.24e-21

DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a glutathione (GSH) dependent enzyme involved in the naphthalene catabolic pathway. It converts HCCA, a hemiketal formed spontaneously after ring cleavage of 1,2-dihydroxynapthalene by a dioxygenase, into cis-o-hydroxybenzylidenepyruvate (cHBPA). This is the fourth reaction in a six-step pathway that converts napthalene into salicylate. HCCA isomerase is unique to bacteria that degrade polycyclic aromatic compounds. It is closely related to the eukaryotic protein, GSH transferase kappa (GSTK).


Pssm-ID: 239320 [Multi-domain]  Cd Length: 192  Bit Score: 84.99  E-value: 6.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335   8 VELFYDVLSPYSWLGFE----ILCRYqniwNINLQLRPSLITGIMKDSGSLS---------------------------- 55
Cdd:cd03022    1 IDFYFDFSSPYSYLAHErlpaLAARH----GATVRYRPILLGGVFKATGNVPpanrppakgryrlrdlerwarrygiplr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335  56 -----------AMRFLTAVNLEHPEMLEKAsRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQaqgLLEKIATPKVKNQ 124
Cdd:cd03022   77 fpprfppntlrAMRAALAAQAEGDAAEAFA-RAVFRALWGEGLDIADPAVLAAVAAAAGLDADE---LLAAADDPAVKAA 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 219842335 125 LKETTEAACRYGAFGLPITVahVDGQthMLFGSDRMELLAHLL 167
Cdd:cd03022  153 LRANTEEAIARGVFGVPTFV--VDGE--MFWGQDRLDMLEEAL 191
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 8-63 3.38e-05

DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins.


Pssm-ID: 239270 [Multi-domain]  Cd Length: 98  Bit Score: 40.85  E-value: 3.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 219842335   8 VELFYDVLSPYSWLGFEILCRYQNI--WNINLQLRPSLITGIMKdSGSLSAMRFLTAV 63
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYAddGGVRVVYRPFPLLGGMP-PNSLAAARAALAA 57
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 7-171 9.07e-04

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 38.33  E-value: 9.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335   7 TVELFYDVLSPYSWLGFEILCRYQNIWNINL-------QLRPSL--------------------------ITGIMKDSG- 52
Cdd:COG2761    3 KIDIFSDVVCPWCYIGKRRLEKALAEFGDDVeirwrpfELNPDMppegedrreyllakgspeqaeqmrahVEEAAAEEGl 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842335  53 -----------SLSAMRFLTAVNLE--HPEMLEKasreLWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEkiaTP 119
Cdd:COG2761   83 pfdfdrikppnTFDAHRLLKAAELQgkQDALLEA----LFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLE---SD 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 219842335 120 KVKNQLKETTEAACRYGAFGLPITVahVDGQtHMLFGSDRMELLAHLLGEKW 171
Cdd:COG2761  156 EAAAAVRADEAEARELGVTGVPTFV--FDGK-YAVSGAQPYEVFEQALRQAL 204
 
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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