The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold.

Publisher: BioMed Central Country of Publication: England NLM ID: 100965194 Publication Model: Electronic Cited Medium: Internet ISSN: 1471-2105 (Electronic) Linking ISSN: 14712105 NLM ISO Abbreviation: BMC Bioinformatics Subsets: MEDLINE

Original Publication: [London] : BioMed Central, 2000-

Helix-Loop-Helix Motifs*/physiology ; Proteasome Endopeptidase Complex*; Multienzyme Complexes/*chemistry; Amino Acid Sequence ; Animals ; Anopheles/chemistry ; Arabidopsis Proteins/chemistry ; Arabidopsis Proteins/physiology ; COP9 Signalosome Complex ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/physiology ; Consensus Sequence ; Drosophila Proteins/chemistry ; Drosophila Proteins/physiology ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; Multienzyme Complexes/physiology ; Multiprotein Complexes ; Neurospora crassa/chemistry ; Nuclear Proteins ; Peptide Hydrolases/chemistry ; Peptide Hydrolases/physiology ; Phylogeny ; Protein Kinases/chemistry ; Protein Kinases/physiology ; Protein Serine-Threonine Kinases/chemistry ; Protein Serine-Threonine Kinases/physiology ; Repressor Proteins/chemistry ; Repressor Proteins/physiology ; Ribonucleoproteins/chemistry ; Ribonucleoproteins/physiology ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/physiology ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/physiology ; Sequence Alignment/methods

Background: Multimeric protein complexes have a role in many cellular pathways and are highly interconnected with various other proteins. The characterization of their domain composition and organization provides useful information on the specific role of each region of their sequence.
Results: We identified a new module, the PAM domain (PCI/PINT associated module), present in single subunits of well characterized multiprotein complexes, like the regulatory lid of the 26S proteasome, the COP-9 signalosome and the Sac3-Thp1 complex. This module is an around 200 residue long domain with a predicted TPR-like all-alpha-helical fold.
Conclusions: The occurrence of the PAM domain in specific subunits of multimeric protein complexes, together with the role of other all-alpha-helical folds in protein-protein interactions, suggest a function for this domain in mediating transient binding to diverse target proteins.

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0 (Arabidopsis Proteins)
0 (CSN2 protein, Arabidopsis)
0 (Cell Cycle Proteins)
0 (Drosophila Proteins)
0 (Macromolecular Substances)
0 (Multienzyme Complexes)
0 (Multiprotein Complexes)
0 (Nuclear Proteins)
0 (RPN3 protein, S cerevisiae)
0 (Repressor Proteins)
0 (Ribonucleoproteins)
0 (Saccharomyces cerevisiae Proteins)
0 (Schizosaccharomyces pombe Proteins)
0 (Thp1 protein, S cerevisiae)
EC 2.7.- (Protein Kinases)
EC 2.7.1.- (Sac3 protein kinase)
EC 2.7.11.1 (Protein Serine-Threonine Kinases)
EC 3.4.- (Peptide Hydrolases)
EC 3.4.19.12 (COP9 Signalosome Complex)
EC 3.4.25.1 (Proteasome Endopeptidase Complex)
EC 3.4.99.- (ATP dependent 26S protease)

Date Created: 20031223 Date Completed: 20040610 Latest Revision: 20211203

20250114

PMC319699

10.1186/1471-2105-4-64

14687415