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Items: 14

1.

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 [1]. [1]. 9680481. Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106. Nishida M, Harada S, Noguchi S, Satow Y, Inoue H, Takahashi K;. J Mol Biol 1998;281:135-147. (from Pfam)

Date:
2024-10-16

Family Accession:
NF026184.5
Method:
HMM

2.

Glutathione S-transferase, N-terminal domain

This family is closely related to Pfam:PF02798. (from Pfam)

GO Terms:
Molecular Function:
protein binding (GO:0005515)
Biological Process:
glutathione metabolic process (GO:0006749)
Date:
2024-08-14

Family Accession:
NF024801.5
Method:
HMM

3.

glutathione S-transferase N-terminal domain-containing protein

GO Terms:
Molecular Function:
protein binding (GO:0005515)
Biological Process:
glutathione metabolic process (GO:0006749)
Date:
2024-08-14

Family Accession:
NF024809.5
Method:
HMM

4.

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 recognised); 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 recognised). 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 [1]. [1]. 9680481. Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106. Nishida M, Harada S, Noguchi S, Satow Y, Inoue H, Takahashi K;. J Mol Biol 1998;281:135-147. (from Pfam)

GO Terms:
Molecular Function:
protein binding (GO:0005515)
Biological Process:
glutathione metabolic process (GO:0006749)
Date:
2024-10-16

Family Accession:
NF014816.5
Method:
HMM

5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
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7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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13.

glutathione S-transferase

glutathione S-transferase 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

Date:
2017-02-03

Family Accession:
11487660
Method:
Sparcle

14.

glutathione transferase

Gene:
yfcF
GO Terms:
Biological Process:
glutathione metabolic process (GO:0006749)
Date:
2021-08-30

Family Accession:
NF011693.0
Method:
HMM

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