| Description | Prismane (hybrid-cluster) proteins are present in a wide range of bacteria and archaea, and are characterised by their two Fe/S centres: a [4Fe-4S] cubane cluster, and a hybrid [4Fe-2S-2O]cluster [ ]. Prismane proteins contain four domains: two spectrin repeat-like 3-helical bundle domains, and two α/β domains with Rossmann-fold topology. Several proteins are structurally related to Prismane, including Ni-containing carbon monoxide dehydrogenase (CODH) (lack one of the N-terminal 3-helical bundle domains), the alpha and beta subunits of bifunctional CODH, and the alpha and beta subunits of acetyl-CoA synthetase.This superfamily represents the spectrin repeat-like 3-helical bundle domains, as well as the two α/β domains with Rossmann-fold topology. | Name | Prismane-like superfamily |
| Short Name | Prismane-like_sf | Type | Homologous_superfamily |
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