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Figure 3 | BMC Molecular Biology

Figure 3

From: Mapping and mutation of the conserved DNA polymerase interaction motif (DPIM) located in the C-terminal domain of fission yeast DNA polymerase δ subunit Cdc27

Figure 3

Sequence alignment of Pol1 interacting region from fission yeast Cdc27 and homologues in other eukaryotic species. Conserved residues are boxed. Abbreviations and NCBI sequence accession numbers: Sp (S. pombe, P30261), Sc (S. cerevisiae, P47110), Nc (Neurospora crassa, XP_328704), Ca (Candida albicans, EAK99562), Gz (Gibberella zeae, XP_384433), Um (Ustilago maydis, XP_401381), Cn (Cryptococcus neoformans, EAL21672), Dh (Debaryomyces hansenii, CAG87841), Dm (Drosophila melanogaster, AAD38629), Ss (Sus scrofa, BF078337), Mm (Mus musculus, Q9EQ28), Rn (Rattus norvegicus, XP_215011), Cf (Canis familiaris, CF411342), Hs (Homo sapiens, Q15054), Ci (Ciona intestinalis, AK114729), Fr (Fugu rubripes, protein sequence derived by translation of clone M001240 at http://fugu.hgmp.mrc.ac.uk/), Tn (Tetraodon nigroviridis, CAF97746), Dr (Danio rerio, AAH76031), Xl (Xenopus laevis, BAC82197), Att (Ambystoma tigrinum tigrinum, CN059104), Gg (Gallus gallus, BU121824 – note the additional glutamate residue within the DPIM), Ce (C. elegans, Q21730), Os (Oryza sativa, NP_913217), and At (Arabadopsis thaliana, C96815). Note that in only a few cases (Sp, Sc, Hs, Mm, Xl) have the identities of these putative Cdc27 proteins been confirmed via purification and characterisation of Pol δ. However, all the sequences shown possess a canonical PCNA binding motif at or near their C-terminal ends (Q -- I -- FF), in common with the bone fide Cdc27 proteins.

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