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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | This domain is found at the C-terminal end of Distal tail protein from Lactococcus phage p2 (Dit or Gp15) and similar proteins predominantly found in virus. Dit self-associates as two rings organised back to back, with a central channel allowing DNA ejection through the viral tail. This domain is located at the ring periphery and display a galectin fold [ , ].Distal tail protein (Dit) has a structural role and forms the distal part of the tail. It is organised into two domains, a ring domain that shows a split barrel-like fold and a C-terminal galectin domain. Consecutive Dit N-terminal domains form a tight ring with two layers of β-strands. This ring frames a channel sufficiently large for dsDNA passage [ , ]. This protein is involved in the process of viral genome ejection through the host cell envelope using a long flexible tail mechanism. The distal tail protein forms the distal part of the tail structure and plays a role in DNA ejection. It self-associates as two rings that are arranged back to back, creating a central channel through which the DNA is ejected into the host cell. Additionally, it interacts with the receptor binding protein, facilitating the attachment of the phage to the host cell. At the structural level, the distal tail protein is composed of homohexameric subunits. | Name | Distal tail protein, C-terminal domain |
| Short Name | Dit_C | Type | Domain |
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