v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | This superfamily represents the N-terminal domain of UPF0234 uncharacterised proteins, which includes YajQ.In Pseudomonas syringae, YajQ functions as a host protein involved in the temporal control of bacteriophage Phi6 gene transcription. It has been shown to bind to the phage's major structural core protein P1, most likely activating transcription by acting indirectly on the RNA polymerase. YajQ may remain bound to the phage particles throughout the infection period [ , ]. Earlier, YajQ was characterized as a putative nucleic acid-binding protein based on the similarity of its (ferredoxin-like) three-dimensional topology with that of RNP-like RNA-binding domains [, ].The polypeptide chain of YajQ is folded into two domains with identical folding topology. Each domain has a four-stranded antiparallel β-sheet flanked on one side by two α-helices. This structural motif is a characteristic feature of many RNA-binding proteins [ ]. |
| Short Name | UPF0234_N |