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. 2024 Jun 6;15(7):e01220-24. doi: 10.1128/mbio.01220-24

Fig 4.

Multiple sequence logos, one for HTCS-REC domains and another for typical REC domains, with graphical representations of the amino acid sequence indicating more conserved amino acids aligned with predicted secondary structure.

HTCS-REC domains have highly conserved regions not observed in typical REC domains. Sequence conservation of HTCS-REC domains is illustrated by sequence logos obtained from the profile hidden Markov model of 6908 HTCS proteins in Bacteroides. Secondary structural elements are shown above the logos. Bar graphs below compare the normalized ICs between HTCS-RECs (gray) and the entire REC family from PFAM PF00072 (pink). In addition to highly conserved phosphorylation site residues (asterisks) at the β-α loops, HTCS-RECs display sequence conservation in other regions, such as the α3-β4 loop (red box) and localized positions at α3 and β5 (triangles).