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Search results 1 to 6 out of 6 for Pcf11

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Family
Description: This entry includes Pcf11 and related proteins from animals, fungi and plants.PCF11 is a subunit and essential component of cleavage and polyadenylation factor IA (CF IA), involved in pre-mRNA 3' end processing and in transcription termination [, , ]. It has been reported that PCF11-mediated termination is essential for vertebrate development and its own levels are maintained by an auto-regulatory mechanism involving premature termination of its transcript []. PCF11 binds to Clp1, another subunit of CFIA whose interaction is responsible for maintaining a tight coupling between the Clp1 nucleotide binding subunit and the other components of the polyadenylation machinery [, ].
Protein Domain
Type: Homologous_superfamily
Description: The C-terminal section of cleavage stimulation and termination factor CstF-64 (CSTF2) and its yeast orthologue Rna15 form a discrete structure that is crucial for mRNA 3'-end processing []. This domain interacts with Pcf11 and possibly PC4, thus linking CSTF2 to transcription, transcriptional termination, and cell growth [].
Protein Domain
Type: Domain
Description: The C-terminal section of cleavage stimulation and termination factor CstF-64 (CSTF2) and its yeast orthologue Rna15 form a discreet structure that is crucial for mRNA 3'-end processing []. This domain interacts with Pcf11 and possibly PC4, thus linking CSTF2 to transcription, transcriptional termination, and cell growth [].Proteins containing this domain also include Pti1 protein from budding yeast. Pti1 is an essential component of CPF (cleavage and polyadenylation factor) involved in 3' end formation of snoRNA and mRNA [].
Protein Domain
Type: Domain
Description: This entry represents the Clp1-interacting domain of Pcf11, found towards the C-terminal end of these proteins.PCF11 is a subunit and essential component of cleavage and polyadenylation factor IA (CF IA), involved in pre-mRNA 3' end processing and in transcription termination [, , ]. It has been reported that PCF11-mediated termination is essential for vertebrate development and its own levels are maintained by an auto-regulatory mechanism involving premature termination of its transcript []. PCF11 binds to Clp1, another subunit of CFIA whose interaction is responsible for maintaining a tight coupling between the Clp1 nucleotide binding subunit and the other components of the polyadenylation machinery [, ].
Protein Domain
Type: Domain
Description: The C-terminal domain (CTD) of the large subunit of RNA polymerase II is aplatform for mRNA processing factors and links gene transcription to mRNAcapping, splicing and polyadenylation. CTD recognition is dependent on thephosphorylation state of the CTD itself, which varies during the course oftranscription but has also been linked to the isomerization state of the CTD'sproline residues. Several RNA-processing factors recognise the CTD by means ofa conserved CTD-interacting domain (CID). Factors with CID domains include theserine/arginine-rich-like factors SCAF4 and SCAF8, Nrd1 (which is implicatedin polyadenylation-independent RNA 3'-end formation) and Pcf11. Pcf11 is aconserved and essential subunit of the yeast cleavage factor 1A, which isrequired for 3'-RNA processing and transcription termination [, ].The CID domain is a right-handed superhelix of eight α-helices forming acompact domain. The CID fold closely resembles that of VHSdomains and is related to armadillo-repeat proteins , except for the two amino-terminal helices. Amino acid residuesin the hydrophobic core of the domain are highly conserved across CID domains[, ].
Protein Domain
Type: Homologous_superfamily
Description: This superfamily represents domains with a multi-helical, α-α 2-layered structural fold as found in: the ENTH domain of Epsin; the VHS domain of Hrs, Tom1, and ADP-ribosylation factors; the RPR domain of PCF11 protein; and the N-terminal domain of phosphoinositide-binding clathrin adaptor.The epsin NH2-terminal homology (ENTH) domain is a membrane interacting module composed of a superhelix of α-helices. It is present at the NH2-terminus of proteins that often contain consensus sequences for binding to clathrin coat components and their accessory factors, and therefore function as endocytic adaptors. ENTH domain containing proteins have additional roles in signalling and actin regulation and may have yet other actions in the nucleus. The ENTH domain is structurally similar to the VHS domain.The ENTH domain is approximately 150 amino acids long. The ENTH domain forms a compact globular structure, composed of eight α-helices connected by loops of varying length. Three helical hairpins that are stacked consecutively with a right-handed twist determine the general topology of the domain. This stacking gives the ENTH domain a rectangular appearance when viewed face on. The most highly conserved amino acids fall roughly into two classes: internal residues that are involved in packing and therefore are necessary for structural integrity, and solvent accessible residues that may be involved in protein-protein interactions [].VHS domains are found at the N-termini of select proteins involved in intracellular membrane trafficking. The domain consists of eight helices arranged in a superhelix. The surface of the domain has two main features: a basic patch on one side due to several conserved positively charged residues on helix 3 and a negatively charged ridge on the opposite side, formed by residues on helix 2. Comparison of the two VHS domains and the ENTH domain reveals a conserved surface, composed of helices 2 and 4, that is utilised for protein-protein interactions. In addition, VHS domain-containing proteins are also often localized to membranes. It has therefore been suggested that the conserved positively charged surface of helix 3 in VHS and ENTH domains plays a role in membrane binding [].