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Flywch zinc finger domain

WebFeb 27, 2015 · It is possible that the zinc finger portion of the WRKY domain does share a common ancestry with FLYWCH, GCM1, MULE and BED proteins that ultimately derives from an ancestral C2H2 zinc finger motif . However, our data suggest that “classical” WRKY transcription factors are too divergent to be usefully considered part of a larger … WebFLYWCH: FLYWCH zinc finger domain: 0.29-5: 20.80: 197: 269: WRKY: WRKY DNA -binding domain: 1.8E-38: 139: 21.00: 211: 271: 466. Plant_zn_clust FLYWCH WRKY. References: Plant_zn_clust 17130173 The natural history of the WRKY-GCM1 zinc fingers and the relationship between transcription factors and transposons. Nucleic Acids Res. …

Cells Free Full-Text FLYWCH1, a Multi-Functional Zinc Finger

Webdomain is best known for its role in sequence‐specific DNA‐binding proteins as the zinc finger transcription factor or in protein–protein interaction involved in post‐translation … WebDec 4, 2024 · FLYWCH; FLYWCH zinc finger domain; NM_020912.2 → NP_065963.1 FLYWCH-type zinc finger-containing protein 1 isoform b. Status: VALIDATED. … orchard upholstery belfast https://fchca.org

Human Gene FLYWCH1 (uc010bsv.3) Description and Page Index

WebDescription: Homo sapiens FLYWCH-type zinc finger 1 (FLYWCH1), transcript variant 1, mRNA. Transcript (Including UTRs) ... SIMILARITY: Contains 5 FLYWCH-type zinc fingers. SEQUENCE CAUTION: Sequence=BAB13378.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; MalaCards Disease Associations WebThe original WRKY protein domain has been proposed to have arisen from the GCM1 and FLYWCH zinc finger factors. GCM1 and FLYWCH are proposed ancestral proteins base on their crystal structural similarity to the WRKY domain. Both GCM1 and FLYWCH belong to families of DNA-binding factors found in metazoan. The plant specific NAC transcription ... WebZinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. This entry represents a potential FLYWCH Zn-finger domain … iptg06a8-4scfkge07

CDD Conserved Protein Domain Family: FLYWCH_N

Category:The GAGA factor regulatory network: Identification of GAGA factor ...

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Flywch zinc finger domain

SMART: Pfam domain FLYWCH

WebAug 4, 2009 · Solution structure of the fifth FLYWCH domain of FLYWCH-type zinc finger-containing protein 1. Released: 04 Aug 2009. DOI: 10.2210/pdb2rpr/pdb. Source organism: Homo sapiens. Entry authors: Enomoto M, Saito K, Tochio N, Kigawa T, Yokoyama S, Nameki N Function and Biology Details. Biochemical function: WebDescription: Homo sapiens FLYWCH-type zinc finger 1 (FLYWCH1), transcript variant 2, mRNA. Transcript (Including UTRs) Position: hg19 chr16:2,961,980-2,990,158 Size ...

Flywch zinc finger domain

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WebProduct Pages: Species: Gene Names: Gene Aliases: RefSeq Accessions: SNP IDs (if applicable): Mature Names (if applicable): 114762 details, 114762 search: Human ... WebMar 23, 2024 · The classical zinc finger domain (also called Cys2His2) that represents the most common class, uses two cysteines and two histidines to coordinate the metal ion, and forms a compact ββα architecture consisting in a β-sheet and an α-helix. GAG-knuckle resembles the classical ZF, treble clef and zinc ribbon are also well represented in the ...

WebFLYWCH: FLYWCH zinc finger domain: 0.23-4: 20.80: 94: 163: WRKY: WRKY DNA -binding domain: 1.9E-08: 38: 21.00: 121: 165: 246. WRKY FLYWCH WRKY. References: WRKY 10785665 The WRKY superfamily of plant transcription factors. Trends Plant Sci 2000;5:199-206. FLYWCH 12723696 The modifier of mdg4 locus in Drosophila: … http://cbsusrv04.tc.cornell.edu/users/ppdb_domain/hmmpfam.aspx?id=666211&eval=1

A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn ) in order to stabilize the fold. It was originally coined to describe the finger-like appearance of a hypothesized structure from the African clawed frog (Xenopus laevis) transcription factor IIIA. However, it has been found to encompass a wide variety of differing protein st… WebHowever, BTB proteins containing the FLYWCH zinc finger domain and the members of the BTB-BACK-PHR subfamily were predicted to be located in the cytosol. The members …

WebFLYWCH is a C2H2-type zinc finger characterised by five conserved hydrophobic residues, containing the conserved sequence motif: In molecular biology, the FLYWCH …

WebInterPro 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. orchard uptown condosWeb5,351 transcription cofactor Silencer Select Pre-designed, Validated, and Custom siRNA in Standard, HPLC, and In-vivo Ready Purities. iptg06ase8-4pn0f11WebZinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. This entry represents a potential FLYWCH Zn-finger domain … orchard v lee 2009 caWebSep 12, 2024 · In molecular biology, the FLYWCH zinc finger is a zinc finger domain. It is found in a number of eukaryotic proteins. FLYWCH is a C2H2-type zinc finger … iptg synthesisWebProduct Pages: Species: Gene Names: Gene Aliases: RefSeq Accessions: SNP IDs (if applicable): Mature Names (if applicable): 108982 details, 108982 search: Human ... iptg06ase14-5sn0f7http://pfam-legacy.xfam.org/family/FLYWCH iptg thermoWebNov 10, 2004 · Glutathione SH-transferase (GST) is a 25-kDa protein and a member of a large family that plays a critical role in the cellular homeostasis of all organisms. In this report, we describe a novel GST-containing protein identified and cloned from Drosophila. This 1045 amino acid protein possesses a zinc finger domain with a tandem array of … orchard uob branch