Malate dehydrogenase (NAD); Catalyzes the reversible oxidation of malate to oxaloacetate. Exhibits higher specific activity for oxaloacetate reduction than for malate oxidation in vitro. Has a strong preference for NAD. Can use NADPH for oxaloacetate reduction, but activity decreases more than 90%. No activity detected with NADP(+) and malate. Belongs to the LDH/MDH superfamily.

GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.

TATA binding protein of transcription factor TFIID; 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.

Methionine aminopeptidase, type II; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.

Translation elongation factor 2 (EF-2/EF-G); Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. [...]

Prefoldin, alpha subunit; Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding.

TIGRFAM: thermosome; PFAM: chaperonin Cpn60/TCP-1; KEGG: pai:PAE3273 thermosome (chaperonin) beta subunit.

TOPRIM domain protein; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteropolymeric, adenine-rich transcripts and the exosome.