PROSITE documentation PDOC51411
PSP1 C-terminal domain profile


The yeast polymerase suppressor 1 (PSP1) protein partially suppresses mutations in DNA polymerases α and delta [1]. The C-terminal half of PSP1 contains a domain, which is also found in several hypothetical proteins from both eukaryotic and prokaryotic sources:

  • Crithidia fasciculata RBP45 and RBP33, subunits of the cycling sequence binding protein (CSBP) II. RBP45 and RBP33 proteins bind specifically to the cycling sequences present in several mRNAs that accumulate periodically during the cell cycle. RBP45 and RBP33 are phosphoproteins, which are phosphorylated differentially during progression through the cell cycle. Hypothetical proteins with high sequence similarity have been identified in other kinetoplastid organisms [2].
  • Bacillus subtilis yaaT protein, which plays a significant role in phosphorelay during initiation of sporulation. It is possible that the yaaT protein is also related to DNA replication. The sequence of the yaaT protein is widely conserved in prokaryotes (bacteria and archaea), but the functions of the protein are unknown [3].

The actual biological significance of the PSP1 C-terminal domain has not yet been clearly established.

The profile we developed covers the entire PSP1 C-terminal domain.

Last update:

November 2008 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

PSP1_C, PS51411; PSP1 C-terminal domain profile  (MATRIX)


1AuthorsFormosa T. Nittis T.
TitleSuppressors of the temperature sensitivity of DNA polymerase alpha mutations in Saccharomyces cerevisiae.
SourceMol. Gen. Genet. 257:461-468(1998).
PubMed ID9529527

2AuthorsMittra B. Ray D.S.
TitlePresence of a poly(A) binding protein and two proteins with cell cycle-dependent phosphorylation in Crithidia fasciculata mRNA cycling sequence binding protein II.
SourceEukaryot. Cell 3:1185-1197(2004).
PubMed ID15470247

3AuthorsHosoya S. Asai K. Ogasawara N. Takeuchi M. Sato T.
TitleMutation in yaaT leads to significant inhibition of phosphorelay during sporulation in Bacillus subtilis.
SourceJ. Bacteriol. 184:5545-5553(2002).
PubMed ID12270811

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