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. 2013 Apr 12;8(4):e57267. doi: 10.1371/journal.pone.0057267

Figure 4. CmHIF1 subunits share high sequence similarity with homologues.

Figure 4

Shown are protein sequences deduced from full length cDNAs of (A) CmHIF1α ) (GenBank accession number JN228344) and (B) CmHIF1β (GenBank accession number JN228345). For both α and β subunits, the bHLH, domains, and PAS-A and PAS-B regions are marked with lines above sequences. The boundaries of the PAS domains are indicated by bent arrows. The CmHIF1α-specific ODD (oxygen-dependent degradation) domain, NAD (N-terminal transactivation domain) and CAD (C-terminal transactivation domain) are also indicated by bent arrows and lines above the sequences, respectively. Prolyl and asparaginyl residues predicted to be hydroxylated by prolyl- and asparaginyl-hydroxylases are marked by asterisks. DmSima (GenBank accession number U43090), HsHIF-1α (U22431) and CeHIF-1 (NM_001028270) are HIF-1α members from D. melanogaster, H. sapiens and C. elegans. Similarly, DmTango (AF020426), HsARNT (M69238) and CeAHA-1 (AF039569) are respective HIF-1β members from the above species. Amino acid residues identical across all sequences are shaded black, and identical across some sequences are shaded grey.