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

TraF protein undergoes proteolytic processing associated with export. The 19 amino acids at the amino terminus of the polypeptides appear to constitute a typical membrane leader peptide - not included in this family, while the remainder of the molecule is predicted to be primarily hydrophilic in character [1]. F plasmid TraF and TraH are required for F pilus assembly and F plasmid transfer, and they are both localised to the outer membrane in the presence of the complete F transfer region, especially TraV, the putative anchor [2]. [1]. 3042757. The product of the F plasmid transfer operon gene, traF, is a periplasmic protein. Wu JH, Kathir P, Ippen-Ihler K;. J Bacteriol. 1988;170:3633-3639. [2]. 20081027. F plasmid TraF and TraH are components of an outer membrane complex involved in conjugation. Arutyunov D, Arenson B, Manchak J, Frost LS;. J Bacteriol. 2010;192:1730-1734. (from Pfam)

Gene:

traF

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

thioredoxin TrxC (aka thioredoxin 2) functions as a thiol disulfide reductase that catalyzes the reduction of protein disulfide bonds in substrates such as ribonucleotide reductase using an active site dithiol, present in a CXXC motif

Date:

2018-09-28

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