EMAP domain-containing protein; PFAM: Putative tRNA binding domain.

PFAM: Ribosomal protein L16p/L10e; TIGRFAM: ribosomal protein L10.e; Belongs to the universal ribosomal protein uL16 family.

Ribosomal protein S7/S5; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center; Belongs to the universal ribosomal protein uS7 family.

Metallohydrolase, glycoprotease/Kae1 family; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function. In the N-terminal section; belongs to the KAE1 / TsaD family.

Ribosomal protein S4/S9; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.

Translation initiation factor eIF-5A; Functions by promoting the formation of the first peptide bond; Belongs to the eIF-5A family.

DNA-directed RNA polymerase, alpha subunit/40 kD subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoD/eukaryotic RPB3 RNA polymerase subunit family.

tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily.

Translation elongation factor aEF-2; 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. EF-G/EF [...]