Protein Family Models

This entry represents the N-terminal domain of thioredoxin 2, which is a zinc finger domain, unusual in thioredoxin proteins [1,2]. Thio2 reduces disulfide bonds and is an efficient electron donor for the essential enzyme ribonucleotide reductase. This domain may mediate protein-protein interactions [1]. [1]. 17913712. Crystal structure of an unusual thioredoxin protein with a zinc finger domain. Ye J, Cho SH, Fuselier J, Li W, Beckwith J, Rapoport TA;. J Biol Chem. 2007;282:34945-34951. [2]. 12952960. Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. Collet JF, D'Souza JC, Jakob U, Bardwell JC;. J Biol Chem. 2003;278:45325-45332. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise. (from Pfam)

Date:

2024-08-14

Trx-GI (thioredoxin of the Genomic Island called the locus of heat resistance) occurs as part of mobile element that is almost present in the rare highly heat-resistant isolate of E. coli or related species. The contribution of Trx-GI to the resistance phenotype is small and poorly understood.

Gene:

trx-GI

Date:

2018-12-13

Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this HMM. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin.

Gene:

trxA

Date:

2024-06-12

Gene:

trxC

Date:

2021-08-23