Belongs to the eukaryotic ribosomal protein eL8 family.
Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.
Part of the 50S ribosomal subunit. Probably part of the RNase P complex.
Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.
Belongs to the histone-like Alba family.
Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.
Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB).
Belongs to the complex I 20 kDa subunit family.
Belongs to the archaeal histone HMF family.
General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation.
Belongs to the eukaryotic ribosomal protein eS28 family.
Belongs to the snRNP Sm proteins family.
Monomer. Interaction with RNA polymerase subunits RpoF and RpoE is necessary for Tfe stimulatory transcription activity. Able to interact with Tbp and RNA polymerase in the absence of DNA promoter. Interacts both with the preinitiation and elongation complexes.
The winged helix domain is involved in binding to DNA in the preinitiation complex.
Transcription factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Facilitates transcription initiation by enhancing TATA-box recognition by TATA-box-binding protein (Tbp), and transcription factor B (Tfb) and RNA polymerase recruitment. Not absolutely required for transcription in vitro, but particularly important in cases where Tbp or Tfb function is not optimal. It dynamically alters the nucleic acid-binding properties of RNA polymerases by stabilizing the initiation complex and destabilizing elongation complexes. Seems to translocate with the RNA polymerase following initiation and acts by binding to the non template strand of the transcription bubble in elongation complexes.
Lacks conserved residue(s) required for the propagation of feature annotation.
Belongs to the universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily.
Binds 16S rRNA, required for the assembly of 30S particles.
Belongs to the universal ribosomal protein uS9 family.
Belongs to the universal ribosomal protein uS10 family.
Involved in the binding of tRNA to the ribosomes.
Belongs to the eukaryotic ribosomal protein eL42 family.