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Research works show that N-terminal and full-length DrrA shows AMPylators activity toward host's Rab1b protein (Ras related protein), which is also the substrate of Rab1b GEF domain. Rab1b protein is the GTPase Rab to regulate vesicle transportation and membrane fusion. The adenylation by bacteria AMPylators prolong GTP-bound state of Rab1b.
Its catalytic domain is homologous to that of other polymerases. [79] It is presumed that the horizontal transfer of bacterial CCA-adding enzyme to eukaryotes allowed the archaeal-like CCA-adding enzyme to switch function to a poly(A) polymerase. [82] Some lineages, like archaea and cyanobacteria, never evolved a polyadenylate polymerase. [94]
The adenylation domain (A) is the focus for substrate specificity since it is the initiating and substrate recognition domain. In one example, adenylation substrate-binding pocket (defined by 10 residue within) alignments led to clusters giving rise to defined specificity (i.e. the residues of the enzyme pocket can predict nonribosomal peptide ...
Uba2 subunit is 640 aa residues long with a molecular weight of 72 kDa. [8] It consists of three domains: an adenylation domain (containing adenylation active site), a catalytic Cys domain (containing the catalytic Cys173 residue participated in thioester bond formation), and a ubiquitin-like domain.
[8] 160 kDa has three β-propeller domains and a C-terminal domain. CPSF-30 (30 kDa) has five Cys-Cys-Cys-His (CCCH) zinc-finger motifs near the N terminus and a CCCH zinc knuckle at the C terminus. Two isoforms of CPSF-30 exist and can be found in CPSF complexes. The RNA binding activity of CPSF-30 is mediated by its zinc-fingers 2 and 3.
The extended peptide is now attached to the current PCP-domain. Condensation-Cyclization: Sometimes the C-domain is replaced by a Cy-domain, which, in addition to the amide bond formation, catalyzes the reaction of the serine, threonine, or cysteine sidechain with the amide-N, thereby forming oxazolidines and thiazolidine, respectively.
Regulation of bacterial glutamine synthase (GlnA) by adenylylation and (indirectly) by uridylylation.Uridylyltransferase (GlnD) uridylylates the regulatory PII protein (GlnB) which determines whether adenylyltransferase (GlnE) adenylylates or de-adenylylates glutamine synthase.
Within the biosynthetic pathway, there are total of five modules that specifically recognize, activate, and condense the amino acids to gramicidin S. Starting module GrsA consists of three domains: Adenylation (A) domain where it incorporates the amino acid and activates it by adenylation using ATP, Thiolation (T) domain or peptidyl carrier ...