AT4G21990.1 :

DomainDescriptionEvalueBitsGAStartEnd
GlutaredoxinGlutaredoxin0.68020.907696
PAPS_reductPhosphoadenosine phosphosulfate reductase family014320.60112292
Thioredoxin_6Thioredoxin-like domain0.75-127.00341360
OST3_OST6OST3 / OST6 family9.4E-061521.30345453
Thioredoxin_7Thioredoxin-like3.4E-051427.00361391
ThioredoxinThioredoxin1.2E-144422.10362454
TraFF plasmid transfer operon protein1.3E-051523.00363435
AhpC-TSAAhpC/TSA family5.3E-061620.70364415
RedoxinRedoxin7.3E-061521.00364410
Thioredoxin_2Thioredoxin-like domain3.2E-072027.00366433
GlutaredoxinGlutaredoxin0.000321120.90372410
Thioredoxin_6Thioredoxin-like domain0.000221127.00412455

 458

Glutaredoxin
PAPS_reduct
Thioredoxin_6
OST3_OST6
Thioredoxin_7
Thioredoxin
TraF
AhpC-TSA
Redoxin
Thioredoxin_2
Glutaredoxin
Thioredoxin_6


References:

Redoxin

OST3_OST6
7622558 Functional characterization of Ost3p. Loss of the 34-kD subunit of the Saccharomyces cerevisiae oligosaccharyltransferase results in biased underglycosylation of acceptor substrates. J Cell Biol 1995;130:567-577.
10358084 The oligosaccharyltransferase complex from Saccharomyces cerevisiae. Isolation of the OST6 gene, its synthetic interaction with OST3, and analysis of the native complex. J Biol Chem 1999;274:17249-17256.

Thioredoxin

Glutaredoxin

Thioredoxin_2

PAPS_reduct
9261082 Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases. Structure 1997;5:895-906.
7588765 Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur J Biochem 1995;233:347-356.
2250719 ATP sulphurylase activity of the nodP and nodQ gene products of Rhizobium meliloti. Nature 1990;348:644-647.

TraF

AhpC-TSA
8041738 Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc Natl Acad Sci U S A 1994;91:7017-7021.

Thioredoxin_7

Thioredoxin_6