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Dsba-like thioredoxin domain

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 … WebMar 8, 2024 · The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox …

Pfam: Family: DSBA (PF01323)

WebOct 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 … WebNational Center for Biotechnology Information teacher wears same shirt for 40 years https://torontoguesthouse.com

DsbA - Wikipedia

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 … 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 … WebDownload 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 ... teacher wears same outfit for picture day

NCBI Conserved Domain Search

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Dsba-like thioredoxin domain

UniProt

WebNov 24, 2015 · Three subfamilies SelUwere annotated humans,SelU1, SelU2 SelU3.All Sec-containing SelU proteins extracted from NRdatabase belonged SelU1family, though SelU1remains unclear. Prx-like2structure domain pre- sented proteinsimplies thioredoxin-likesuperfamily. Many members SelU1family commonlyreferred C10orf58-likeproteins. 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.

Dsba-like thioredoxin domain

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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 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 formation as peptides emerge into the cell's periplasm. [2] Structurally, DsbA contains a thioredoxin domain with an inserted helical domain of unknown function. [3]

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 WebDec 6, 2005 · DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more …

http://j.bjfu.edu.cn/article/doi/10.12171/j.1000-1522.20240368?viewType=HTML 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 …

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

WebDomain: 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; teacher wears dressWebInstead 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 … teacher wears dress dailyWebDsbA 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 ... teacherweaverWebDsbA introduces disulfide bonds into folding proteins, and is re-oxidized through interaction with its redox partner DsbB. Mycobacterium tuberculosis, a Gram-positive bacterium, … teacher wears scream maskWebDSBA-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]. ... south indian beef fryWebTSTA_124180 DSBA-like thioredoxin domain protein [] Gene ID: 8098369, updated on 26-Jun-2015. Summary. Gene provides a unified query environment for genes defined by sequence and/or in NCBI's Map Viewer. TSTA_124180 DSBA-like thioredoxin domain protein [] Gene ID: 8098369, updated on ... teacher webWebInterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool. teacher web amy mckay