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Fig. 6 | Microbial Cell Factories

Fig. 6

From: Mapping the membrane proteome of anaerobic gut fungi identifies a wealth of carbohydrate binding proteins and transporters

Fig. 6

Domain architecture of gut fungal class C GPCRs identified from transcriptome data. All class C GPCRs are predicted to have a long amino-terminal domain and seven carboxy-terminal transmembrane helices. The amino-terminal domain ranges from 200 to 1600 amino acid residues with the average length being 600 residues. Around 30% of the putative GPCRs are predicted to have an extracellular pectin lyase fold (IPR011050; IPR012334), parallel beta-helix repeats (IPR006626), and/or an EGF-like domain (IPR000742). Around 50% of the GPCRs are predicted to have a domain that is homologous to SBP Type II (a.k.a. Periplasmic binding protein-like II, SCOP superfamily SSF53850). Several putative GPCRs do not have any apparent homology to known InterPro domains. In approximately 30% of the cases we can identify a canonical ER targeting signal peptide at the very aminoterminus (not shown). N amino-terminus. For more details, see Additional file 2: Figure S2

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