Dsba-like thioredoxin domain

Author: mpiy

August undefined, 2024

WebDsbA (EC 1.8.4.15) introduces protein disulfide bonds in the periplasm and transfers the electrons via DsbB (EC 1.8.5.9) to ubiquinone and menaquinone. DsbA has a CPHC … Web类硫氧还蛋白结构域蛋白 DSBA-like thioredoxin domain-containing protein: 9: XP_038974828.1: 生长素响应因子17-like X1亚型 Auxin response factor 17-like isoform X1（ARF） 10: XP_040992987.1: 渗调-like蛋白 Osmotin-like protein: 11: MBA0678152.1: 假定蛋白 Hypothetical protein: 12: XP_022760600.1

Pfam: Family: DSBA (PF01323)

WebDsbA family protein (domain architecture ID 10122501) ... DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif with similarity to DsbA and FrnE. FrnE is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and ... WebGene ID: 13876961, discontinued on 1-Aug-2024. Summary Other designations. DSBA-like thioredoxin domain protein rounding serum creatinine in elderly patients

Structural and biochemical characterization of the …

WebGene ID: 103641494, discontinued on 13-May-2024 Summary DISCONTINUED: This record has been withdrawn by NCBI staff. This record represented a gene that is not currently annotated by NCBI. Other designations DSBA-like thioredoxin domain containing protein http://pfam-legacy.xfam.org/family/PF01323 WebInstead of forming a separate domain as in DsbA, the inserted residues of glutathione peroxidase wind around the thioredoxin fold to produce the tetramer interface, part of which forms a fifth strand in the thioredoxin fold 3-sheet … rounding second base

CDD Conserved Protein Domain Family: DSBA - National …

Thioredoxin domain - Wikipedia

WebMar 1, 2016 · DsbA harbors a canonical thioredoxin-like fold that is characterized by an N-terminal βαβ motif and a C-terminal ββα motif . However, unlike thioredoxin, these motifs are separated by an extended α-helical domain. The DsbA active site is composed of a reactive disulfide bond found in a CXXC ... Webthiol:disulfide interchange protein DsbA/DsbL (domain architecture ID 10122479) thiol:disulfide interchange protein DsbA/DsbL is involved in disulfide bond formation and it functions by transferring its disulfide bond to other proteins. Graphical summary. Zoom to … straub auto repair hastingsWebDownload scientific diagram Thioredoxin-like, DsbA-like and redox domains in the ER from publication: Calnexin cycle ‐ structural features of the ER chaperone system The endoplasmic ... straub automotive weather eye

"WebDomain: IPR001853: DSBA-like thioredoxin domain: Family: IPR014371: Sterol O-acyltransferase, ACAT/DAG/ARE types: Family: IPR014440: HCCA isomerase/glutathione S-transferase kappa: Homologous_superfamily: IPR036249: Thioredoxin-like superfamily: Domain Details Per Protein . Protein Length " - Dsba-like thioredoxin domain

Dsba-like thioredoxin domain

CDD Conserved Protein Domain Family: Thioredoxin_like

WebIPR001853 DSBA-like_thioredoxin_dom IPR023205 DsbA/DsbL IPR036249 Thioredoxin-like_sf IPR017937 Thioredoxin_CS IPR013766 Thioredoxin_domain PIRSF PIRSF001488 Tdi_protein 1 hit PROSITE View protein in PROSITE PS00194 THIOREDOXIN_1 1 hit PS51352 THIOREDOXIN_2 1 hit Pfam View protein in Pfam … http://j.bjfu.edu.cn/article/doi/10.12171/j.1000-1522.20240368?viewType=HTML

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WebDsbA introduces disulfide bonds into folding proteins, and is re-oxidized through interaction with its redox partner DsbB. Mycobacterium tuberculosis, a Gram-positive bacterium, … WebDsbA_GSTK domain-containing protein (domain architecture ID 10122488) DsbA_GSTK domain-containing protein. Graphical summary. Zoom to residue level ... Refine search. List of domain hits. Name: Accession: Description: Interval: E-value: DsbA_GSTK: cd03021: DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a …

WebDsbA is a bacterial thiol disulfide oxidoreductase (TDOR). DsbA is a key component of the Dsb (disulfide bond) family of enzymes. DsbA catalyzes intrachain disulfide bond … WebDSBA-like thioredoxin domain Provide feedback. This family contains a diverse set of proteins with a thioredoxin-like structure PF00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyse one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways [2,3,4]. ...

WebNational Center for Biotechnology Information WebSep 1, 2024 · Aims: DsbA catalyzes disulfide bond formation in secreted and outer membrane proteins in bacteria. In pathogens, DsbA is a major facilitator of virulence …

WebThe formation of disulphide bonds is an essential step in the folding of many proteins that enter the secretory pathway; therefore, it is not surprising that eukaryotic and prokaryotic organisms have dedicated enzymatic systems to catalyse this process. In bacteria, one such enzyme is disulphide bond-forming protein A (DsbA), a thioredoxin-like thiol oxidase …

WebThe thiol/disulfide oxidoreductase DsbA is the strongest oxidant of the thioredoxin superfamily and is required for efficient disulfide bond formation in the periplasm of Escherichia coli. straub automotive wheeling wvWebDSBA-like thioredoxin domain (DSBA) DSBA-like thioredoxin domain: This family contains a diverse set of proteins with a thioredoxin-like structure Pfam:PF00085. This … rounding shapes in substance designerWebDomain: 20-150: Thioredoxin PROSITE-ProRule annotation. BLAST Add. ... IPR001853 DSBA-like_thioredoxin_dom; IPR023205 DsbA/DsbL; IPR036249 Thioredoxin-like_sf; IPR017937 Thioredoxin_CS; IPR013766 Thioredoxin_domain; PIRSF. PIRSF001488 Tdi_protein 1 hit; PROSITE. View protein in PROSITE; PS00194 THIOREDOXIN_1 1 hit; straub at the highlandsWebSep 29, 2024 · DSBA-like thioredoxin domain. This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in … straub automotive wheeling west virginiaWebDsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in ... rounding sheets medicine straub beer alcohol contentWebOct 18, 2013 · The X-ray crystal structure of Mt-DsbA reveals a two-domain structure, comprising a canonical thioredoxin domain with the conserved CXXC active site … straub beer nutrition information