The $Sec61{alpha}$ subunit is the core subunit of the protein conducting channel which is required for protein translocation in eukaryotes and prokaryotes. In this study, we cloned a $Sec61{alpha}$ subunit from Penicillium ochrochloron ($PoSec61{alpha}$). Sequence and 3D structural model analysis showed that $PoSec61{alpha}$ conserved the typical characteristics of eukaryotic and prokaryotic $Sec61{alpha}$ subunit homologues. The pore ring known as the constriction point of the channel is formed by seven hydrophobic amino acids. Two methionine residues from transmembrane ${alpha}$-helice 7 (TM7) contribute to the pore ring formation and projected notably to the pore area and narrowed the pore compared with the superposed residues at the corresponding positions in the crystal structures or the 3D models of the $Sec61{alpha}$ subunit homologues in archaea or other eukaryotes, respectively. Results reported herein indicate that the pore ring residues differ among $Sec61{alpha}$ subunit homologues and two hydrophobic residues in the TM7 contribute to the pore ring formation.