Fusion of the shell and cargo protein of a type 1 encapsulin nanocompartment. Protein missing its signal peptide makes 33 nm particles in E.coli (called cEnc), protein missing its signal peptide and diheme domain (residues 1-86, called Enc) makes 29 nm particles. The cEnc nancompartment encloses c-type heme. The cargo protein NIR-HAO (AC P0DV45) is probably targeted to the nanocompartment by its association with the diheme domain in cEnc; removal of the diheme domain in Enc halves the amount of cargo. Binds 2 heme groups per molecule. The encapsulin nanocompartment is probably formed by 180 monomers, with the N-terminus (diheme domain) inside (Probable). There are 36 pores where the pentamers meet as well as 3-fold axis channels and dimer channels (By similarity). This type 1 encapsulin nanocompartment may be targeted to the anammoxosome. In (PubMed:28263314) the signal peptide was removed prior to generating the constructs for expression in E.coli. Belongs to the encapsulin family. Family 1 subfamily.