Summary: C-terminal domain of 1-Cys peroxiredoxin
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C-terminal domain of 1-Cys peroxiredoxin Provide feedback
This is the C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols . The C-terminal domain is crucial for providing the extra cysteine necessary for dimerisation of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine, upstream of this domain; and glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulfide to the sulfhydryl and consequent activation of the enzyme . The domain is associated with family AhpC-TSA, PF00578 which carries the catalytic cysteine.
Manevich Y, Feinstein SI, Fisher AB; , Proc Natl Acad Sci U S A. 2004;101:3780-3785.: Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST. PUBMED:15004285 EPMC:15004285
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This tab holds annotation information from the InterPro database.
InterPro entry IPR019479
This entry represents the C-terminal domain of 1-Cys peroxiredoxin, a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols [PUBMED:9587003]. The C-terminal domain is crucial for providing the extra cysteine necessary for dimerisation of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine found upstream of this domain. Glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulphide to the sulphydryl and consequent activation of the enzyme [PUBMED:15004285]. The domain is associated with INTERPRO, which carries the catalytic cysteine.
|Molecular function||peroxiredoxin activity (GO:0051920)|
|Biological process||oxidation-reduction process (GO:0055114)|
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|Seed source:||Gene3D, pdb_1prx|
|Author:||Finn RD, Coggill PC|
|Number in seed:||84|
|Number in full:||20884|
|Average length of the domain:||33.70 aa|
|Average identity of full alignment:||46 %|
|Average coverage of the sequence by the domain:||16.62 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the 1-cysPrx_C domain has been found. There are 523 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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